NTPPA_ACIAD
ID NTPPA_ACIAD Reviewed; 183 AA.
AC Q6FDX8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=dTTP/UTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528};
DE Short=dTTPase/UTPase {ECO:0000255|HAMAP-Rule:MF_00528};
DE EC=3.6.1.9 {ECO:0000255|HAMAP-Rule:MF_00528};
DE AltName: Full=Nucleoside triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528};
DE AltName: Full=Nucleotide pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528};
DE Short=Nucleotide PPase {ECO:0000255|HAMAP-Rule:MF_00528};
GN OrderedLocusNames=ACIAD0829;
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1;
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP
CC and UTP. May have a dual role in cell division arrest and in preventing
CC the incorporation of modified nucleotides into cellular nucleic acids.
CC {ECO:0000255|HAMAP-Rule:MF_00528}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00528}.
CC -!- SIMILARITY: Belongs to the Maf family. YhdE subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00528}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR543861; CAG67730.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6FDX8; -.
DR SMR; Q6FDX8; -.
DR STRING; 62977.ACIAD0829; -.
DR EnsemblBacteria; CAG67730; CAG67730; ACIAD0829.
DR KEGG; aci:ACIAD0829; -.
DR eggNOG; COG0424; Bacteria.
DR HOGENOM; CLU_040416_2_1_6; -.
DR OMA; RIDGDFY; -.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0036221; F:UTP diphosphatase activity; IEA:RHEA.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00555; Maf; 1.
DR Gene3D; 3.90.950.10; -; 1.
DR HAMAP; MF_00528; Maf; 1.
DR InterPro; IPR029001; ITPase-like_fam.
DR InterPro; IPR003697; Maf-like.
DR PANTHER; PTHR43213; PTHR43213; 1.
DR Pfam; PF02545; Maf; 1.
DR PIRSF; PIRSF006305; Maf; 1.
DR SUPFAM; SSF52972; SSF52972; 1.
DR TIGRFAMs; TIGR00172; maf; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Nucleotide metabolism; Reference proteome.
FT CHAIN 1..183
FT /note="dTTP/UTP pyrophosphatase"
FT /id="PRO_0000267236"
FT ACT_SITE 64
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 7
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 65
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
FT SITE 147
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528"
SQ SEQUENCE 183 AA; 20215 MW; E219487F2C9008CE CRC64;
MASSSPRRQE LLKQLGLEFE SYAPEIDESV QYNETVEAYV ERLAREKANT ILQQFPQSII
IAADTSLSID GKIIGKPESK QHAFDIWSTL SGRRHDVFSG ICVAASNAIH SCVVKTSVEF
QTLSMADMEL YWATGEPLGK AGAYAIQGIA AQFIPRIEGS YTNVVGLPLF ETIQLLKRVK
AFN
